Evidence map›Paper›PMID 32053881›Full record

ArticleBiomolecules2020

Role of an Aromatic-Aromatic Interaction in the Assembly and Trafficking of the Zebrafish Panx1a Membrane Channel.

Ksenia Timonina, Anna Kotova, Georg Zoidl

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 41% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Endocytosis of Connexin 36 is Mediated by Interaction with Caveolin-1.International journal of molecular sciences · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ksenia TimoninaDepartment of Biology, York University, Ontario M3J 1P3, Canada.
Anna KotovaDepartment of Biology, York University, Ontario M3J 1P3, Canada.
Georg ZoidlDepartment of Biology, York University, Ontario M3J 1P3, Canada.
York University · CA

Funding

Natural Sciences and Engineering Research Council of Canada GZ-XXX
6 · The paper itself

Abstract

Pannexin 1 (Panx1) is a ubiquitously expressed hexameric integral membrane protein known to function as an adenosine triphosphate (ATP) release channel. Panx1 proteins exist in unglycosylated core form (Gly0). They undergo critical post-translational modifications forming the high mannose glycosylation state (Gly1) in the endoplasmic reticulum (ER) and the complex glycosylation state (Gly2) in the Golgi apparatus. The regulation of transition from the ER to the cell membrane is not fully understood. Using site-specific mutagenesis, dye uptake assays, and interaction testing, we identified two conserved aromatic residues, Trp123 and Tyr205, in the transmembrane domains 2 and 3 of the zebrafish panx1a protein

Indexed as

Amino Acids, AromaticAnimalsCell Line, TumorCell MembraneConnexinsEndoplasmic ReticulumGlycosylationGolgi ApparatusMiceMutagenesis, Site-DirectedMutant ProteinsProtein FoldingProtein MultimerizationProtein Processing, Post-TranslationalProtein StabilityProtein TransportAmino Acids, AromaticConnexinsMutant Proteinspanx1a protein, zebrafishZebrafish Proteinsco-localizationFRAPFRETintegral membrane proteinN-glycosylationpannexinprotein traffickingstructure–function

Identifiers

PMID32053881
PMCPMC7072349
OpenAlexW3005671090

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.